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Extended-spectrum beta-lactamases: structure and kinetic mechanism.

Page, M G P.

Clin Microbiol Infect ; 14 Suppl 1: 63-74, 2008 Jan.

Article in English | MEDLINE | ID: mdl-18154529

ABSTRACT

Recent years have seen an explosion in the numbers of extented spectrum class A beta-lactamases (ESBLs). The steady-state kinetic parameters for hydrolysis of beta-lactams by ESBLs is discussed in the light of what is known about the structure of these mutant enzymes.

Subject(s)

Gram-Negative Bacteria/enzymology , beta-Lactamases/chemistry , beta-Lactamases/metabolism , beta-Lactams/metabolism , Gram-Negative Bacteria/genetics , Humans , Hydrolysis , Kinetics , Models, Molecular , Mutation , Protein Conformation , Structure-Activity Relationship , Substrate Specificity , beta-Lactamase Inhibitors , beta-Lactamases/genetics , beta-Lactams/chemistry , beta-Lactams/classification

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